EFN4_CAEEL
ID EFN4_CAEEL Reviewed; 348 AA.
AC O44516;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Ephrin-4;
DE AltName: Full=Protein male abnormal 26;
DE Flags: Precursor;
GN Name=efn-4; Synonyms=mab-26; ORFNames=F56A11.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=12403719; DOI=10.1242/dev.00122;
RA Chin-Sang I.D., Moseley S.L., Ding M., Harrington R.J., George S.E.,
RA Chisholm A.D.;
RT "The divergent C. elegans ephrin EFN-4 functions in embryonic morphogenesis
RT in a pathway independent of the VAB-1 Eph receptor.";
RL Development 129:5499-5510(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP IDENTIFICATION, AND NOMENCLATURE.
RX PubMed=10635316; DOI=10.1016/s1097-2765(00)80220-8;
RA Wang X., Roy P.J., Holland S.J., Zhang L.W., Culotti J.G., Pawson T.;
RT "Multiple ephrins control cell organization in C. elegans using kinase-
RT dependent and -independent functions of the VAB-1 Eph receptor.";
RL Mol. Cell 4:903-913(1999).
RN [4]
RP FUNCTION.
RX PubMed=12679110; DOI=10.1016/s0012-1606(02)00129-x;
RA Hahn A.C., Emmons S.W.;
RT "The roles of an ephrin and a semaphorin in patterning cell-cell contacts
RT in C. elegans sensory organ development.";
RL Dev. Biol. 256:379-388(2003).
RN [5]
RP FUNCTION.
RX PubMed=15030761; DOI=10.1016/s1534-5807(04)00057-7;
RA Ikegami R., Zheng H., Ong S.-H., Culotti J.G.;
RT "Integration of semaphorin-2A/MAB-20, ephrin-4, and UNC-129 TGF-beta
RT signaling pathways regulates sorting of distinct sensory rays in C.
RT elegans.";
RL Dev. Cell 6:383-395(2004).
RN [6]
RP FUNCTION, INTERACTION WITH LAD-2, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP 328-SER--TYR-348.
RX PubMed=26903502; DOI=10.1242/dev.128934;
RA Dong B., Moseley-Alldredge M., Schwieterman A.A., Donelson C.J.,
RA McMurry J.L., Hudson M.L., Chen L.;
RT "EFN-4 functions in LAD-2-mediated axon guidance in Caenorhabditis
RT elegans.";
RL Development 143:1182-1191(2016).
CC -!- FUNCTION: Regulates the formation or stabilization of cell-cell
CC contacts at several stages of epithelial morphogenesis
CC (PubMed:12679110). In early embryonic development, involved in ventral
CC closure of the epidermis (PubMed:12403719). During male tail
CC morphogenesis, regulates precursor cell sorting together with mab-20
CC and allows the formation of distinct sensory rays (PubMed:15030761).
CC Probably acts as a ligand for lad-2 to regulate axon guidance of
CC several neurons including SDQL, SDQR, SMD and PLN neurons during
CC neurogenesis (PubMed:26903502). {ECO:0000269|PubMed:12403719,
CC ECO:0000269|PubMed:12679110, ECO:0000269|PubMed:15030761,
CC ECO:0000269|PubMed:26903502}.
CC -!- SUBUNIT: Interacts with lat-2. {ECO:0000269|PubMed:26903502}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the developing nervous system
CC (PubMed:12403719). Expressed in head and tail neurons, nerve ring,
CC ventral nerve cord, lateral neurons, CAN neuron, seam cells and vulva
CC cells (PubMed:26903502). {ECO:0000269|PubMed:12403719,
CC ECO:0000269|PubMed:26903502}.
CC -!- PTM: May undergo proteolysis by metalloprotease sup-17 to give rise to
CC a soluble form. {ECO:0000305|PubMed:26903502}.
CC -!- DISRUPTION PHENOTYPE: Worms have widespread defects in embryonic
CC morphogenesis of the posterior body and defects in postembryonic male
CC tail morphogenesis. {ECO:0000269|PubMed:12403719}.
CC -!- MISCELLANEOUS: In contrast to other ephrins, does not seem to signal
CC through the vab-1 receptor. {ECO:0000269|PubMed:12403719}.
CC -!- SIMILARITY: Belongs to the ephrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00884}.
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DR EMBL; AF410936; AAL05561.1; -; mRNA.
DR EMBL; FO080624; CCD65257.1; -; Genomic_DNA.
DR PIR; T32645; T32645.
DR RefSeq; NP_499947.1; NM_067546.4.
DR AlphaFoldDB; O44516; -.
DR SMR; O44516; -.
DR BioGRID; 42043; 6.
DR STRING; 6239.F56A11.3; -.
DR EPD; O44516; -.
DR PaxDb; O44516; -.
DR EnsemblMetazoa; F56A11.3.1; F56A11.3.1; WBGene00001165.
DR GeneID; 176882; -.
DR KEGG; cel:CELE_F56A11.3; -.
DR UCSC; F56A11.3; c. elegans.
DR CTD; 176882; -.
DR WormBase; F56A11.3; CE29503; WBGene00001165; efn-4.
DR eggNOG; KOG3858; Eukaryota.
DR GeneTree; ENSGT00970000196527; -.
DR HOGENOM; CLU_779010_0_0_1; -.
DR InParanoid; O44516; -.
DR OMA; FVCPDNE; -.
DR OrthoDB; 1247864at2759; -.
DR PhylomeDB; O44516; -.
DR Reactome; R-CEL-3928662; EPHB-mediated forward signaling.
DR Reactome; R-CEL-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-CEL-3928664; Ephrin signaling.
DR Reactome; R-CEL-3928665; EPH-ephrin mediated repulsion of cells.
DR SignaLink; O44516; -.
DR PRO; PR:O44516; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001165; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0046875; F:ephrin receptor binding; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0042074; P:cell migration involved in gastrulation; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:WormBase.
DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:WormBase.
DR GO; GO:1902667; P:regulation of axon guidance; IMP:UniProtKB.
DR GO; GO:0030155; P:regulation of cell adhesion; IMP:WormBase.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR031328; Ephrin.
DR InterPro; IPR001799; Ephrin_RBD.
DR PANTHER; PTHR11304; PTHR11304; 1.
DR Pfam; PF00812; Ephrin; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR PROSITE; PS51551; EPHRIN_RBD_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Disulfide bond; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Neurogenesis; Reference proteome;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..329
FT /note="Ephrin-4"
FT /id="PRO_0000248550"
FT PROPEP 330..348
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000248551"
FT DOMAIN 21..178
FT /note="Ephrin RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT REGION 207..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 329
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT DISULFID 79..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT MUTAGEN 328..348
FT /note="Missing: No defect in SDQL axon migration. Restores
FT SDQL axon migration in a sup-17 (n316) mutant background."
FT /evidence="ECO:0000269|PubMed:26903502"
SQ SEQUENCE 348 AA; 39593 MW; 851E9EB07C0048FF CRC64;
MKQFFEFLIT TFLLLGLAAA DEHIVYWNST NSLFRNRQPT IEVRMGDVVR FVCPDNEEGR
NDGEYLIVYE VTEFAMDDCA LESHSREVIR CAPEGTAEKV LRTQQLSGGR REDWKKQKVP
PKNVAQLIRQ LNPIPNGKEY QPGQTYYYMT TSTGKANGTN HRMYGLCESQ NMRLSMKVSA
SQPHPTRRAP TRRQEDFVTT ASAELMGGQE DEDSDNDNAH LLPRDLEGST NPKFRRPSQL
ETAGVENQQF MKVVQMAQAG KTGTFENEKE AIAQKSSEKD GWHPVNVQYV ADLMNNAYQN
ADERISYQRD FEIHEENDLA VKSLEYSSSS TSLSTNFAIL LAVIYVLY
